3061-90-3

Basic information

• Product Name: H-ALA-PHE-OH
• Synonyms: L-ALA-PHE;L-ALANYL-L-PHENYLALANINE;H-ALA-PHE-OH;ALA-PHE;alanylphenylalanine;L-alanyl-phenylalanine;(S)-2-[[(S)-2-Aminopropionyl]amino]-3-phenylpropionic acid;Ala-Phe-OH
• CAS NO: 3061-90-3
• Molecular Formula: C₁₂H₁₆N₂O₃
• Molecular Weight: 236.27
• EINECS: 217-885-6
• Product Categories: Dipeptides;Dipeptides and Tripeptides;Peptides
• Mol File: 3061-90-3.mol

Chemical Properties

• Boiling Point: 487.6 °C at 760 mmHg
• Flash Point: 248.7 °C
• Appearance: /Solid
• Density: 1.222
• Refractive Index: 1.565
• Storage Temp.: −20°C
• PKA: 3.41±0.10(Predicted)
• CAS DataBase Reference: H-ALA-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-ALA-PHE-OH(3061-90-3)
• EPA Substance Registry System: H-ALA-PHE-OH(3061-90-3)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 3061-90-3(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-ALA-PHE-OH is used as an active pharmaceutical ingredient for its potential therapeutic applications. As a dipeptide, it can be utilized in the development of drugs targeting various health conditions due to its bioavailability and ability to be absorbed by the body.
Used in Cosmetic Industry:
H-ALA-PHE-OH is used as an ingredient in the cosmetic industry for its potential benefits in skincare products. The dipeptide may contribute to skin health and rejuvenation, making it a valuable component in anti-aging and skin care formulations.
Used in Research and Development:
H-ALA-PHE-OH is used as a research compound for studying the properties and potential applications of dipeptides in various scientific fields. Its unique structure allows researchers to explore its interactions with other molecules and its effects on biological systems.
Used in Nutritional Supplements:
H-ALA-PHE-OH can be used as an ingredient in nutritional supplements, particularly those aimed at enhancing athletic performance, muscle recovery, and overall health. The dipeptide may provide benefits such as improved nitrogen retention and muscle growth.
Used in Food Industry:
H-ALA-PHE-OH may be used in the food industry as a flavor enhancer or additive due to its dipeptide structure. It can potentially improve the taste and texture of various food products, making it a valuable component in the development of new and improved food items.

InChI:InChI=1/C12H16N2O3/c1-8(13)11(15)14-10(12(16)17)7-9-5-3-2-4-6-9/h2-6,8,10H,7,13H2,1H3,(H,14,15)(H,16,17)/t8-,10?/m0/s1

Upstream product

• 63-91-2 L-phenylalanine 
• 16964-94-6 (S)-4-methyl-thiazolidine-2,5-dione 
• 1738-73-4 α-Alanyl-phenylalaninbenzylester 
• 18979-06-1 H-Ala-Phe-NH₂ 
• 103-72-0 phenyl isothiocyanate 
• 121574-54-7 Ac-Ala-DAPA-Ala-Phe-OH 
• 121574-46-7 N²-(N-Ac-L-Ala)-L-2,4-diaminobutanoyl-L-Ala-L-Phe 
• 105995-30-0 N-Ac-L-Ala-L-Gln-L-Ala-L-Phe 
• 100431-45-6 N-<(R)-2-(aminocarbonyl)-1-oxopropyl>-L-phenyl alanine 
• 2543-29-5 Cbz-L-ala-L-phe-Cbz 
• 25172-67-2 Z-Ala-O-COO-isoBu 
• 16874-17-2 L-phenylalanine tert-butyl ester 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 2448-58-0 (S)-2-((S)-2-((tert-butoxycarbonyl)amino)propanamido)-3-phenylpropanoic acid 

Downstream Products

• 134423-82-8 Dns-Ala-Phe 
• 79410-44-9 dicyclohexylammonium N-(L-2-azidopropionyl)-L-phenylalaninate 
• 1738-73-4 α-Alanyl-phenylalaninbenzylester 
• 56672-76-5 1-hippuroyl-L-proline 
• 40298-89-3 L-alanyl-L-phenylalanine methyl ester 
• 952312-44-6 methyl acryloyl-L-alanyl-L-phenylalanine 
• 1262797-20-5 N',N-bis(Boc)-N-guanidine Ala-Phe 
• 63-91-2 L-phenylalanine 
• 56-41-7 L-alanin 
• 26698-64-6 L-alanyl-L-alanyl-L-phenylalanine 
• 84759-79-5 2-[(S)-1-((S)-1-Methoxycarbonyl-2-phenyl-ethylcarbamoyl)-ethylamino]-3-methyl-butyric acid methyl ester 

Relevant articles and documents

Hydrolytic cleavage of pyroglutamyl-peptide bond. III. A highly selective cleavage in 70% methanesulfonic acid

A method for highly selective cleavage of pGlu-peptide linkages in 70% methanesulfonic acid (MSA) is described. When pGlu-Ala-Phe-OH, pGlu-His-Pro- OH and dog neuromedin U-8 (d-NMU-8) (1-7)-OH (pGlu-Phe-Leu-Phe-Arg-Pro-Arg- OH) were hydrolyzed in 70% MSA at 60°C for 3 h or at 25°C for 3 d, the pGlu-peptide linkage was predominantly cleaved to give H-Ala-Phe-OH, H-His- Pro-OH and H-Phe-Leu-Phe-Arg-Pro-Arg-OH, in high yields. The results indicated that pGlu-peptide linkages are highly susceptible to 70% MSA, whereas the amide bond of the pyrrolidone moiety of the pGlu residue and other internal peptide bonds are extremely resistant.

A dynamic combinatorial library for biomimetic recognition of dipeptides in water

Small peptides are involved in countless biological processes. Hence selective binding motifs for peptides can be powerful tools for labeling or inhibition. Finding those binding motifs, especially in water which competes for intermolecular H-bonds, poses an enormous challenge. A dynamic combinatorial library can be a powerful method to overcome this issue. We previously reported artificial receptors emerging form a dynamic combinatorial library of peptide building blocks. In this study we aimed to broaden this scope towards recognition of small peptides. Employing CXC peptide building blocks, we found that cyclic dimers of oxidized CFC bind to the aromatic peptides FF and YY (K ≈ 229-702 M-1), while AA binds significantly weaker (K ≈ 65-71 M-1).

Highly Productive Continuous Flow Synthesis of Di- and Tripeptides in Water

The reaction of amino acid derived N-carboxyanhydrides (NCAs) with unprotected amino acids under carefully controlled aqueous continuous flow conditions realized the formation of a range of di- and tripeptide products in 60-85% conversion at productivities of up to 535 g·L-1h-1. This required a fundamental understanding of the physicochemical aspects of the reaction resulting in the design of a custom-made continuous stirred tank reactor (CSTR) with continuous solids addition, high shear mixing, automated pH control to avoid the use of buffer, and efficient heat removal to control the reaction at 1 ± 1 °C.

Coupling-Reagent-Free Synthesis of Dipeptides and Tripeptides Using Amino Acid Ionic Liquids

A general method for the synthesis of dipeptides has been developed, which does not require any coupling reagents. This method is based on the reaction of readily available HCl salts of amino acid methyl esters with tetrabutylphosphonium amino acid ionic liquids. The isolation procedure of stepwise treatment with AcOH is easy to carry out. The method was extended to the synthesis of tripeptide, tyrosyl-glycyl-glycine, present in IMREG-1, also.

A green route for the synthesis of a bitter-taste dipeptide combining biocatalysis, heterogeneous metal catalysis and magnetic nanoparticles

There is increasing demand for green technologies to produce high-solubility and low-toxicity compounds with potential application in the food industry. This study aimed to establish a clean, synthetic route for preparing the bitter-taste dipeptide Ala-Phe, a potential substitute for caffeine as a food additive. Synthesis of Z-Ala-Phe-OMe starting from Z-Ala-OH and HCl·Phe-OMe was catalysed by thermolysin at 50 °C in buffer (step 1). Z-Ala-Phe-OMe ester hydrolysis to give Z-Ala-Phe-OH at 37 °C in 30% acetonitrile/buffer was catalysed by α-bovine chymotrypsin (αCT), protease with esterase activity (step 2). Hydrogenation of Z-Ala-Phe to give the desired Ala-Phe was catalysed by C/Pd in methanol (step 3). Steps 2 and 3 were optimized by using the magnetically recoverable recycling enzyme Fe3O4@silica-αCT and the magnetically recoverable metal nanocatalyst Fe3O4@silica-Pd, respectively. This inspiring combination of technologies and the original results demonstrate the suitability of using enzymes, metal catalyst and magnetic nanoparticles for easy, economical, stereoselective, clean production of an important target compound. Besides, they add to the development of peptide chemistry and catalysis.

Redox-triggered changes in the self-assembly of a ferrocene-peptide conjugate

Ultrasonication of a ferrocene conjugate of a short amyloid peptide (Aβ18-20) in toluene causes formation of an organogel, which undergoes dramatic structural changes upon oxidation from a nanofibrillar network to spherical micelles. This morphological change is redox-controlled and reversible. the Partner Organisations 2014.

Direct asymmetric intermolecular aldol reactions catalyzed by amino acids and small peptides

In nature there are at least nineteen different acyclic amino acids that act as the building blocks of poly-peptides and proteins with different functions. Here we report that α-amino acids, β-amino acids, and chiral amines containing primary amine functions catalyze direct asymmetric intermolecular aldol reactions with high enantio-selectivities. Moreover, the amino acids can be combined into highly modular natural and unusual small peptides that also catalyze direct asymmetric intermolecular aldol reactions with high stereoselectivities, to furnish the corre sponding aldol products with up to > 99% ee. Simple amino acids and small peptides can thus catalyze asymmetric aldol reactions with stereoselectivities matching those of natural enzymes that have evolved over billions of years. A small amount of water accelerates the asymmetric aldol reactions catalyzed by amino acids and small peptides, and also increases their stereoselectivities. Notably, small peptides and amino acid tetrazoles were able to catalyze direct asymmetric aldol reactions with high enantioselectivities in water, while the parent amino acids, in stark contrast, furnished nearly racemic products. These results suggest that the prebiotic oligomerization of amino acids to peptides may plausibly have been a link in the evolution of the homochirality of sugars. The mechanism and stereochemistry of the reactions are also discussed.

Small peptides as modular catalysts for the direct asymmetric aldol reaction: Ancient peptides with aldolase enzyme activity

Simple peptides and their analogues having a primary amino group as the catalytic residue mediate the direct asymmetric intermolecular aldol reaction with high stereoselectivity and furnish the corresponding aldol products with up to 99% ee; this intrinsic ability of highly modular peptides may explain the initial molecular evolution of aldolase enzymes. The Royal Society of Chemistry 2005.

Carbamoylation of amino groups in peptides via N-aryloxycarbonyl intermediates

Method of synthesising peptides containing one or more amino acid residues bearing an N-carbamoyl functional group, by aminolysis of N-aryloxycarbonyl derivatives, which are excellent synthesis intermediates for the preparation of various peptides containing amino acid residues bearing a ureino group, such as citrulline, homocitrulline, 2-amino-4-ureidobutyric residues.

Hydrolytic cleavage of pyroglutamyl-peptide bond. II. effects of amino acid residue neighboring the pglu moiety

We studied the susceptibility of the pyrrolidone moiety and the pyroglutamyl-peptide bond at pGlu-X-Ala-Phe-OH (X = Gly, Ala, Tyr, Ile, Pro, His, Lys, Arg, Thr, Ser, Asp, Glu and Trp) to 1N HCl or 2M trifluoromethanesulfonic acid at 60°C. Here we describe the rates of the cleavage reaction of the pGlu-X bond, the pyrrolidone ring-opening reaction of the pGlu moiety and the hydrolysate accumulation. The rank order of the susceptibility rates of the cleavage reactions was Ser > Pro, Gly > Arg, Ala, Glu, Thr, Asp > His, Lys > Trp, Tyr, Ile, and that of the ring-opening reaction was Ile > Tyr, Trp > Arg, His, Lys, Asp > Glu > Ala > Pro, Gly > Ser > Thr. The rank order of the half-lives of the model peptides was Pro > Arg, Lys, Ile > His, Glu > Ala, Tyr > Asp > Gly > Ser > Thr. The results indicated that a bulky and sterically hindered side chain of the amino acid residue neighboring the pGlu moiety favors the ring-opening reaction, and retards the decomposition on acid hydrolysis and the cleavage reaction. Thus, the ring-opening and the cleavage reactions were greatly affected by the amino acid residue neighboring the pGlu moiety in the hydrolysis of pGlu-peptides.